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Journal of Virology, February 2000, p. 1383-1392, Vol. 74, No. 3
Department of Medical Microbiology and
Immunology, University of Wisconsin, Madison, Wisconsin 53706
Received 6 October 1999/Accepted 19 October 1999
Glycoprotein B (gB; gpUL55) of human cytomegalovirus (HCMV) plays a
critical role in virus entry and cell-to-cell spread of infection. To
define the structure-function relationships in gB, a panel of
linker-insertion mutations was generated throughout the coding region.
This strategy yielded a panel of 22 mutants with four amino acid
insertions and 3 large truncation mutants. Assessment of the mutant
proteins' biosynthetic properties and folding patterns analyzed in
context with predicted secondary features revealed novel insights into
gB's structure and trafficking properties. All of the insertion
mutants were able to assemble into oligomers, suggesting that
oligomerization is tolerant of small insertions and/or that multiple
regions of the protein may be involved. Computer algorithm predictions
of gB's secondary structure indicate that the furin-recognized
cleavage site falls within an exposed loop. This loop may be
particularly sensitive to structural alterations, since insertions
upstream and downstream of the cleavage site rendered the mutant
proteins cleavage defective. In addition, a strong correlation existed
between terminal folding and cleavage of gB. Interestingly, terminal
folding was not correlated with delivery to the cell surface but may
influence the rate of transport to the cell surface. Nine mutants,
containing insertions in both the extracellular and intracellular
portions of gB, retained wild-type structural properties. This panel of
characterized gB mutants, the first of this type for an HCMV protein,
will be a useful tool in dissecting the role of gB during HCMV infection.
0022-538X/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.
Characterization of a Panel of Insertion Mutants in
Human Cytomegalovirus Glycoprotein B
*
Corresponding author. Mailing address: Department of
Medical Microbiology and Immunology, University of Wisconsin, Madison, WI 53706. Phone: (608) 262-1474. Fax: (608) 262-8418. E-mail: tcompton{at}facstaff.wisc.edu.
Journal of Virology, February 2000, p. 1383-1392, Vol. 74, No. 3
0022-538X/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.
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